3WGM

STAPHYLOCOCCUS AUREUS FTSZ T7 mutant substituted for GAN bound with GTP, DeltaT7GAN-GTP

Summary for 3WGM

• Entry DOI: 10.2210/pdb3wgm/pdb
• Related: 3WGJ 3WGK 3WGL 3WGN 3voa
• Descriptor: Cell division protein FtsZ, GUANOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: ftsz, gtp-binding, tubulin homolog, polymerization, gtpase, cell division, cell cycle
• Biological source: Staphylococcus aureus
• Cellular location: Cytoplasm (By similarity): P0A029
• Total number of polymer chains: 2
• Total formula weight: 83154.49

Authors

Han, X.,Matsui, T.,Yu, J.,Tanaka, I.,Yao, M. (deposition date: 2013-08-06, release date: 2013-12-25, Last modification date: 2023-11-08)

Primary citation

Matsui, T.,Han, X.,Yu, J.,Yao, M.,Tanaka, I.
Structural change in FtsZ Induced by intermolecular interactions between bound GTP and the T7 loop
J.Biol.Chem., 289:3501-3509, 2014

PubMed Abstract: FtsZ is a prokaryotic homolog of tubulin and is a key molecule in bacterial cell division. FtsZ with bound GTP polymerizes into tubulin-like protofilaments. Upon polymerization, the T7 loop of one subunit is inserted into the nucleotide-binding pocket of the second subunit, which results in GTP hydrolysis. Thus, the T7 loop is important for both polymerization and hydrolysis in the tubulin/FtsZ family. Although x-ray crystallography revealed both straight and curved conformations of tubulin, only a curved structure was known for FtsZ. Recently, however, FtsZ from Staphylococcus aureus has been shown to have a very different conformation from the canonical FtsZ structure. The present study was performed to investigate the structure of FtsZ from Staphylococcus aureus by mutagenesis experiments; the effects of amino acid changes in the T7 loop on the structure as well as on GTPase activity were studied. These analyses indicated that FtsZ changes its conformation suitable for polymerization and GTP hydrolysis by movement between N- and C-subdomains via intermolecular interactions between bound nucleotide and residues in the T7 loop.

PubMed: 24347164
DOI: 10.1074/jbc.M113.514901

Experimental method

X-RAY DIFFRACTION (2.091 Å)